EP0550599B1 - Peptide zur verwendung in impfung und anregung von antikörperbildung gegen menschliches immunschwäche virus - Google Patents
Peptide zur verwendung in impfung und anregung von antikörperbildung gegen menschliches immunschwäche virus Download PDFInfo
- Publication number
- EP0550599B1 EP0550599B1 EP91917502A EP91917502A EP0550599B1 EP 0550599 B1 EP0550599 B1 EP 0550599B1 EP 91917502 A EP91917502 A EP 91917502A EP 91917502 A EP91917502 A EP 91917502A EP 0550599 B1 EP0550599 B1 EP 0550599B1
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- European Patent Office
- Prior art keywords
- peptide
- amino acid
- peptides
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- hiv
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/18—Antivirals for RNA viruses for HIV
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2740/00—Reverse transcribing RNA viruses
- C12N2740/00011—Details
- C12N2740/10011—Retroviridae
- C12N2740/16011—Human Immunodeficiency Virus, HIV
- C12N2740/16111—Human Immunodeficiency Virus, HIV concerning HIV env
- C12N2740/16122—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
Definitions
- peptides gp120-12 amino acid coordinates 159-183
- gp120-19 amino acid coordinates 255-276
- peptide gp120-19 is similar to a peptide that has been described (Ho et al., Science, 239:1021-1023 (1988)), it has now been found that gp120-19 elicits neutralizing antibodies in primates.
- the peptides of the present invention can be used as immunogens in vaccine composition and to elicit polyclonal or monoclonal antibody production; particularly important are HIV neutralizing antibodies.
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- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Virology (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Public Health (AREA)
- Biochemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oncology (AREA)
- Veterinary Medicine (AREA)
- Gastroenterology & Hepatology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Communicable Diseases (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- AIDS & HIV (AREA)
- Tropical Medicine & Parasitology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Claims (8)
- Verfahren zur Herstellung eines Peptids mit mindestens einem Epitop, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, und mit der Aminosäuresequenz:wobei X ausgewählt ist aus der Gruppe bestehend aus einem Wasserstoffatom der aminoterminalen NH2-Gruppe des Peptids und einer weiteren Aminosäure, ausgewählt um die Kopplung des Peptids an einen Träger zu erleichtern; Y abwesend oder Cystein ist und Z ausgewählt ist aus der Gruppe bestehend aus der Carboxyl-Gruppe der carboxyterminalen Aminosäure und einer Amidogruppe, umfassend das Synthetisieren des Peptids durch bekannte Festphasen-Peptidsynthesetechniken.
- Verfahren zur Herstellung eines Peptids mit mindestens einem Epitop, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, und mit der Aminosäuresequenz:umfassend das Synthetisieren des Peptids durch bekannte Festphasen-Peptidsynthesetechniken.
- Verfahren zur Herstellung eines Peptids mit mindestens einem Epitop, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, und mit der Aminosäuresequenz:wobei X ausgewählt ist aus der Gruppe bestehend aus einem Wasserstoffatom der aminoterminalen NH2-Gruppe des Peptids und einer weiteren Aminosäure, ausgewählt um die Kopplung des Peptids an einen Träger zu erleichtern; Y abwesend oder Cystein ist und Z ausgewählt ist aus der Gruppe bestehend aus der Carboxyl-Gruppe der carboxyterminalen Aminosäure und einer Amidogruppe, umfassend das Synthetisieren des Peptids durch bekannte Festphasen-Peptidsynthesetechniken.
- Verfahren zur Herstellung eines Peptids mit mindestens einem Epitop, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, und mit der Aminosäuresequenz:umfassend des Synthetisieren des Peptids durch bekannte Festphasen-Peptidsynthesetechniken.
- Verfahren zur Herstellung einer Vakzinzusammensetzung, umfassend eine immunologisch wirksame Menge eines Peptids mit mindestens einem Epitop, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, und mit der Aminosäuresequenz:und einen physiologisch verträglichen Träger dafür, wobei X ausgewählt ist aus der Gruppe bestehend aus einem Wasserstoffatom der aminoterminalen NH2-Gruppe des Peptids und einer weiteren Aminosäure, ausgewählt um die Kopplung des Peptids an einen Träger zu erleichtern; Y abwesend oder Cystein ist und Z ausgewählt ist aus der Gruppe bestehend aus der Carboxyl-Gruppe der carboxyterminalen Aminosäure und einer Amidogruppe, umfassend das Formulieren der immunologisch wirksamen Menge des Peptids mit einem physiologisch verträglichen Träger.
- Verfahren zur Herstellung einer Vakzinzusammensetzung, umfassend eine immunologisch wirksame Menge eines Peptids mit mindestens einem Epitop, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, und mit der Aminosäuresequenz:und Analoge und Homologe davon und ein physiologisch verträglicher Träger dafür, wobei Z ausgewählt ist aus der Gruppe bestehend aus einem Wasserstoffatom der aminoterminalen NH2-Gruppe des Peptids und einer weiteren Aminosäure, ausgewählt um die Kopplung des Peptids an einen Träger zu erleichtern, umfassend das Formulieren der immunologisch wirksamen Menge des Peptids mit einem physiologisch verträglichen Träger.
- Verfahren zur Herstellung einer Vakzinzusammensetzung, umfassend eine immunologisch wirksame Menge von mindestens zwei Peptiden, wobei jedes der Peptide mindestens ein Epitop besitzt, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, eines der Peptide die Aminosäuresequenz besitzt:und mindestens ein anderes Peptid ausgewählt ist aus der Gruppe von Peptiden mit den Aminosäuresequenzen:
und
und einen physiologisch verträglicher Träger dafür, wobei X ausgewählt ist aus der Gruppe bestehend aus einem Wasserstoffatom der aminoterminalen NH2-Gruppe des Peptids und einer weiteren Aminosäure, ausgewählt um die Kopplung des Peptids an einen Träger zu erleichtern; Y abwesend oder Cystein ist und Z ausgewählt ist aus der Gruppe bestehend aus der Carboxyl-Gruppe der carboxyterminalen Aminosäure und einer Amidogruppe, umfassend das Formulieren der immunologisch wirksamen Mengen der mindestens zwei Peptide mit dem physiologisch verträglichen Träger.
- Verfahren zur Herstellung einer Vakzinzusammensetzung, umfassend eine immunologisch wirksame Menge von mindestens zwei Peptiden, wobei jedes der Peptide mindestens ein Epitop besitzt, das von Antikörpern erkannt wird, die spezifisch für das menschliche Immunschwächevirus sind, eines der Peptide die Aminosäuresequenz besitzt:und mindestens ein anderes Peptid ausgewählt ist aus der Gruppe von Peptiden mit den Aminosäuresequenzen:
und einen physiologisch verträglicher Träger dafür, wobei X ausgewählt ist aus der Gruppe bestehend aus einem Wasserstoffatom der aminoterminalen NH2-Gruppe des Peptids und einer weiteren Aminosäure, ausgewählt um die Kopplung des Peptids an einen Träger zu erleichtern; Y abwesend oder Cystein ist und Z ausgewählt ist aus der Gruppe bestehend aus der Carboxyl-Gruppe der carboxyterminalen Aminosäure und einer Amidogruppe, umfassend das Formulieren der immunologisch wirksamen Mengen der mindestens zwei Peptide mit dem physiologisch verträglichen Träger.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US58942290A | 1990-09-27 | 1990-09-27 | |
| US589422 | 1990-09-27 | ||
| PCT/SE1991/000641 WO1992005800A1 (en) | 1990-09-27 | 1991-09-25 | Peptides for use in vaccination and induction of neutralizing antibodies against human immunodeficiency virus |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| EP0550599A1 EP0550599A1 (de) | 1993-07-14 |
| EP0550599B1 true EP0550599B1 (de) | 2003-04-23 |
Family
ID=24357953
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| EP91917502A Expired - Lifetime EP0550599B1 (de) | 1990-09-27 | 1991-09-25 | Peptide zur verwendung in impfung und anregung von antikörperbildung gegen menschliches immunschwäche virus |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US5589175A (de) |
| EP (1) | EP0550599B1 (de) |
| JP (1) | JPH06501260A (de) |
| AT (1) | ATE238065T1 (de) |
| AU (1) | AU650911B2 (de) |
| CA (1) | CA2091263C (de) |
| DE (1) | DE69133242T2 (de) |
| ES (1) | ES2194836T3 (de) |
| FI (1) | FI931393A0 (de) |
| HU (1) | HU9300877D0 (de) |
| MC (1) | MC2308A1 (de) |
| OA (1) | OA09802A (de) |
| WO (1) | WO1992005800A1 (de) |
Families Citing this family (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5939074A (en) * | 1986-12-30 | 1999-08-17 | The United States Of America As Represented By The Department Of Health And Human Services | Multideterminant peptide antigens |
| US5346989A (en) * | 1990-08-22 | 1994-09-13 | Syntello Vaccine Development Kb | Peptides for use in induction of T cell activation against HIV-1 |
| EP0594638A1 (de) * | 1991-06-03 | 1994-05-04 | Syntello Vaccine Development Ab | Peptide zur induktion der t-zell aktivierung gegen hiv-1 |
| JPH07501516A (ja) * | 1991-08-29 | 1995-02-16 | アメリカ合衆国 | ヒトの被験者におけるｈｉｖに反応するヘルパーｔリンパ球を刺激する多重決定基ペプチド抗原 |
| IT1254360B (it) * | 1992-05-11 | 1995-09-14 | San Romanello Centro Fond | Epitopi immunologicamente omologhi di hla e proteine del virus hiv. |
| DE4228787A1 (de) * | 1992-08-29 | 1994-03-03 | Chemotherapeutisches Forschungsinstitut Georg Speyer Haus | Neue HIV-1-Virusisolate eines Subtyps, Vakzine gegen HIV-1-Virusinfektionen dieses Subtyps und Verfahren zu ihrer Herstellung, Verwendung der HIV-1-Virusisolate |
| AU6515394A (en) * | 1993-04-16 | 1994-11-08 | Syntello Vaccine Development Ab | Peptides for use in vaccination and induction of neutralizing antibodies against human immunodeficiency virus |
| FR2707170A1 (fr) * | 1993-06-04 | 1995-01-13 | Pasteur Institut | Expression des récepteurs CD4 et CD26 dans des cellules recombinantes, inhibiteurs du récepteur CD26. |
| FR2707169B1 (fr) * | 1993-06-04 | 1995-09-01 | Pasteur Institut | Antigène cellulaire CD26 impliqué dans l'infection par un rétrovirus hiv. nouveaux inhibiteurs de l'infection par HIV. * (Dipeptidyl-peptidase IV). |
| DE4405810A1 (de) | 1994-02-23 | 1995-08-24 | Behringwerke Ag | Von einem Retrovirus aus der HIV-Gruppe abgeleitete Peptide und deren Verwendung |
| WO1997039020A2 (en) * | 1996-04-15 | 1997-10-23 | The University Of North Carolina At Chapel Hill | Antigenic sequences of a sperm protein and immunocontraceptive methods |
| WO1999024465A1 (en) * | 1997-11-10 | 1999-05-20 | Dana-Farber Cancer Institute | Stabilized primate lentivirus envelope glycoproteins |
| ES2709176T3 (es) | 2006-08-11 | 2019-04-15 | Life Sciences Res Partners Vzw | Péptidos inmunogénicos y su uso en trastornos inmunitarios |
| EP2623115A1 (de) | 2008-02-14 | 2013-08-07 | Life Sciences Research Partners VZW | Immunogene Beeinflussung von Tumoren und Tumorzellen |
| ES2545886T3 (es) | 2008-02-14 | 2015-09-16 | Life Sciences Research Partners Vzw | Inmunoterapia dirigida a patógenos intracelulares |
| US10023847B2 (en) | 2010-11-25 | 2018-07-17 | Imnate Sarl | Immunogenic peptides for use in the prevention and/or treatment of infectious diseases, autoimmune diseases, immune responses to allofactors, allergic diseases, tumors, graft rejection and immune responses against viral vectors used for gene therapy or gene vaccination |
| GB201201511D0 (en) | 2012-01-30 | 2012-03-14 | Univ Leuven Kath | Modified epitopes for boosting CD4+ T-cell responses |
| GB201309469D0 (en) | 2013-05-28 | 2013-07-10 | Imcyse Sa | Detection of CD4+ T lymphocytes |
| GB201418433D0 (en) | 2014-10-17 | 2014-12-03 | Imcyse Sa | Novel immunogenic peptides |
| US10729791B2 (en) | 2015-05-18 | 2020-08-04 | Imcyse Sa | Animal models for evaluating pharmaceutical compounds |
| CN108289941B (zh) | 2015-09-25 | 2022-06-21 | 易姆赛斯股份公司 | 用于消除对治疗剂的免疫应答的改进的方法和化合物 |
| CN109069605B (zh) | 2016-04-19 | 2022-11-29 | 易姆赛斯股份公司 | 新免疫原性CD1d结合肽 |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3588254T2 (de) * | 1984-10-18 | 2008-06-26 | Institut Pasteur | GAG-Antigen und dessen Verwendung zum Nachweis von LAV-Infektion, sowie in immunogenen Zusammensetzungen |
| WO1987007616A1 (en) * | 1986-06-12 | 1987-12-17 | Biogen N.V. | Peptides involved in the pathogenesis of hiv infection |
| US5128319A (en) * | 1987-08-28 | 1992-07-07 | Board Of Regents, The University Of Texas System | Prophylaxis and therapy of acquired immunodeficiency syndrome |
| US5019387A (en) * | 1987-09-08 | 1991-05-28 | Duke University | Production of antibodies to HIV |
| WO1989005820A1 (en) * | 1987-12-21 | 1989-06-29 | Arch Development Corporation | Hiv-related antigens and antibodies |
| EP0330359A3 (de) * | 1988-02-25 | 1991-06-05 | Bio-Rad Laboratories, Inc. | Zusammensetzung, verwendbar zur Diagnose und Behandlung von HIV-I-Infektion |
| AU3557889A (en) * | 1988-04-20 | 1989-11-24 | Trustees Of The University Of Pennsylvania, The | Protective peptides derived from human immunodeficiency virus-1 gp160 |
| US4943628A (en) * | 1988-06-13 | 1990-07-24 | Ortho Pharmaceutical Corporation | HIV peptide-inducted T cell stimulation |
| CA2078545A1 (en) * | 1990-04-03 | 1991-10-04 | Timothy J. Gregory | Hiv envelope polypeptides |
| AP237A (en) * | 1990-05-29 | 1993-04-29 | Cedars Sinai Medical Center | Immunoreagents reactive with a conserved epitope of human immunodeficiency virus type 1 (HIV-1) gp120 and methods of use. |
| EP0594638A1 (de) * | 1991-06-03 | 1994-05-04 | Syntello Vaccine Development Ab | Peptide zur induktion der t-zell aktivierung gegen hiv-1 |
-
1991
- 1991-09-25 EP EP91917502A patent/EP0550599B1/de not_active Expired - Lifetime
- 1991-09-25 JP JP3516126A patent/JPH06501260A/ja active Pending
- 1991-09-25 HU HU93877A patent/HU9300877D0/hu unknown
- 1991-09-25 ES ES91917502T patent/ES2194836T3/es not_active Expired - Lifetime
- 1991-09-25 AU AU86435/91A patent/AU650911B2/en not_active Ceased
- 1991-09-25 AT AT91917502T patent/ATE238065T1/de not_active IP Right Cessation
- 1991-09-25 WO PCT/SE1991/000641 patent/WO1992005800A1/en active IP Right Grant
- 1991-09-25 DE DE69133242T patent/DE69133242T2/de not_active Expired - Fee Related
- 1991-09-25 CA CA002091263A patent/CA2091263C/en not_active Expired - Fee Related
- 1991-09-27 MC MC912308D patent/MC2308A1/xx unknown
-
1993
- 1993-03-23 OA OA60353A patent/OA09802A/en unknown
- 1993-03-26 FI FI931393A patent/FI931393A0/fi not_active Application Discontinuation
-
1995
- 1995-03-27 US US08/410,384 patent/US5589175A/en not_active Expired - Lifetime
Non-Patent Citations (5)
| Title |
|---|
| CHEMICAL ABSTRACTS, vol. 111, no. 7, 14 August 1989, Columbus, OH (US); T.J. PALKER et al., p. 553, no. 55349m/ * |
| CHEMICAL ABSTRACTS, vol. 112, no. 23, 04 June 1990, Columbus, OH (US); A.R. NEURATH et al., p. 454, no. 214787s/ * |
| ED. DANI BOLOGNESI, "HIV Binding to the CD4 Molecule: Conformation Dependence and Binding Inhibition Studies", 1989; J.S. McDOUGAL et al., pp. 269-281/ * |
| JOURNAL OF ACQUIRED IMMUNE DEFICIENCY SYNDROMES, vol., 2, 1989; S. MODROW et al., pp. 21-27/ * |
| SCIENCE, vol. 239, February 1988; D.D. HO et al., pp. 1021-1023/ * |
Also Published As
| Publication number | Publication date |
|---|---|
| MC2308A1 (fr) | 1993-09-27 |
| HU9300877D0 (en) | 1993-06-28 |
| ES2194836T3 (es) | 2003-12-01 |
| WO1992005800A1 (en) | 1992-04-16 |
| DE69133242D1 (de) | 2003-05-28 |
| AU650911B2 (en) | 1994-07-07 |
| US5589175A (en) | 1996-12-31 |
| AU8643591A (en) | 1992-04-28 |
| DE69133242T2 (de) | 2004-02-19 |
| EP0550599A1 (de) | 1993-07-14 |
| OA09802A (en) | 1994-04-15 |
| CA2091263A1 (en) | 1992-03-28 |
| FI931393A (fi) | 1993-03-26 |
| ATE238065T1 (de) | 2003-05-15 |
| FI931393A0 (fi) | 1993-03-26 |
| JPH06501260A (ja) | 1994-02-10 |
| CA2091263C (en) | 2003-05-06 |
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